Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9Y4K0 (LOXL2_HUMAN)

Entry version 190 (07 Apr 2021)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
Add a publicationFeedback
Protein

Lysyl oxidase homolog 2

Gene

LOXL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (PubMed:27735137). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (PubMed:27735137). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (PubMed:25959397). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (By similarity). Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3 (PubMed:16096638, PubMed:27735137, PubMed:24414204). During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292). Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (PubMed:28332555). Involved in E-cadherin repression following hypoxia, a hallmark of EMT believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression (PubMed:20026874). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:20306300). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity).By similarity8 Publications

Miscellaneous

Its overexpression in a number of cancers and its ability to promote epithelial to mesenchymal transition suggest that LOXL2 might play a role in tumor progression: expression is correlated with metastasis and decreased survival in patients with aggressive breast cancer (PubMed:21233336, PubMed:21732535). Allosteric inhibition by AB0023 inhibits formation of the tumor microenvironment and reduces metastatic tumor burden in xenograft models (PubMed:20818376, PubMed:21732535). However, inhibiting the enzyme activity of LOXL2 may not be sufficient, since inhibition of keratinocyte differentiation is not prevented in mutants that lack enzyme activity nor by inhibition of activity by the AB0023 antibody, thereby promoting development of squamous cell carcinomas (PubMed:22157764).4 Publications

Caution

The original paper reporting the role of LOXL2 in deamination of trimethylated 'Lys-4' of histone H3 was retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this role was confirmed in a subsequent publication (PubMed:27735137).2 Publications1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

According to some reports, it is inhibited by beta-aminopropionitrile (BAPN) (PubMed:20439985 and PubMed:23319596). According to another report, it is not inhibited by beta-aminopropionitrile (BAPN) (PubMed:20306300). Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner.4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2.04 min(-1) with tropoelastin as substrate (without the first three SRCR domains). kcat is 0.62 min(-1) with tropoelastin as substrate (without all four SRCR domains).
  1. KM=1.01 mM for 1,5-diaminopentane2 Publications
  2. KM=1.05 mM for spermine2 Publications
  3. KM=0.59 µM for tropoelastin (without the first three SRCR domains)2 Publications
  4. KM=0.62 µM for tropoelastin (without all four SRCR domains)2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi549Calcium1 Publication1
    Metal bindingi550Calcium; via carbonyl oxygen1 Publication1
    Metal bindingi626Copper1 Publication1
    Metal bindingi628Copper1 Publication1
    Metal bindingi630Copper1 Publication1
    Metal bindingi722Calcium1 Publication1
    Metal bindingi724Calcium; via carbonyl oxygen1 Publication1
    Metal bindingi727Calcium1 Publication1
    Metal bindingi728Calcium1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionChromatin regulator, Oxidoreductase, Repressor
    Biological processTranscription, Transcription regulation
    LigandCalcium, Copper, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.4.3.13, 2681

    Pathway Commons web resource for biological pathway data

    More...    PathwayCommonsi    		Q9Y4K0

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-1566948, Elastic fibre formation
    R-HSA-2243919, Crosslinking of collagen fibrils

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		Q9Y4K0

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Lysyl oxidase homolog 2 (EC:1.4.3.134 Publications)
    Alternative name(s):
    Lysyl oxidase-like protein 2
    Lysyl oxidase-related protein 2
    Lysyl oxidase-related protein WS9-14
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:LOXL2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:6666, LOXL2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		606663, gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q9Y4K0

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...    VEuPathDBi    		HostDB:ENSG00000134013.15

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Basement membrane, Chromosome, Endoplasmic reticulum, Extracellular matrix, Nucleus, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi455N → Q: Inhibits secretion. 1 Publication1
    Mutagenesisi626 – 628HRH → ARA: Abolishes oxidase activity and oxidation of trimethylated 'Lys-4' of histone H3 but does not affect secretion, interaction with SNAI1, binding to the CDH1 promoter, repression of CDH1 transcription or ability to induce EMT. 2 Publications3
    Mutagenesisi626H → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi628H → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi630H → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi644N → Q: Inhibits secretion. 1 Publication1
    Mutagenesisi653K → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi689Y → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi689Y → F: Does not affect ability to inhibit keratinocyte differentiation. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		4017

    Open Targets

    More...    OpenTargetsi    		ENSG00000134013

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA30429

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		Q9Y4K0, Tbio

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3714029

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		2853

    Genetic variation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		LOXL2

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		13878585

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001853226 – 774Lysyl oxidase homolog 2Add BLAST749

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi84 ↔ 148PROSITE-ProRule annotation
    Disulfide bondi97 ↔ 158PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 138PROSITE-ProRule annotation
    Disulfide bondi218 ↔ 291PROSITE-ProRule annotation
    Disulfide bondi231 ↔ 301PROSITE-ProRule annotation
    Disulfide bondi265 ↔ 275PROSITE-ProRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi351 ↔ 414PROSITE-ProRule annotation
    Disulfide bondi364 ↔ 424PROSITE-ProRule annotationCombined sources1 Publication
    Disulfide bondi395 ↔ 405PROSITE-ProRule annotationCombined sources1 Publication
    Glycosylationi455N-linked (GlcNAc...) (complex) asparagine1 Publication1
    Disulfide bondi464 ↔ 530PROSITE-ProRule annotationCombined sources1 Publication
    Disulfide bondi477 ↔ 543PROSITE-ProRule annotationCombined sources1 Publication
    Disulfide bondi511 ↔ 521PROSITE-ProRule annotationCombined sources1 Publication
    Disulfide bondi573 ↔ 625Combined sources1 Publication
    Disulfide bondi579 ↔ 695Combined sources1 Publication
    Glycosylationi644N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki653 ↔ 689Lysine tyrosylquinone (Lys-Tyr)2 Publications
    Disulfide bondi657 ↔ 673Combined sources1 Publication
    Disulfide bondi663 ↔ 685Combined sources1 Publication
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6892',4',5'-topaquinone1 Publication1
    Disulfide bondi732 ↔ 746PROSITE-ProRule annotationCombined sources1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.2 Publications
    N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		Q9Y4K0

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q9Y4K0

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		Q9Y4K0

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		Q9Y4K0

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		Q9Y4K0

    PeptideAtlas

    More...    PeptideAtlasi    		Q9Y4K0

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q9Y4K0

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		86223

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1480, 1 N-Linked glycan (1 site)

    GlyGen: Computational and Informatics Resources for Glycoscience

    More...    GlyGeni    		Q9Y4K0, 3 sites

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q9Y4K0

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		Q9Y4K0

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in many tissues (PubMed:10212285). Highest expression in reproductive tissues, placenta, uterus and prostate (PubMed:10212285). In esophageal epithelium, expressed in the basal, prickle and granular cell layers (PubMed:22204712). Up-regulated in a number of cancers cells and tissues.2 Publications

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Strongly induced in hypoxia. Direct transcriptional target of HIF1A.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000134013, Expressed in stromal cell of endometrium and 194 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		Q9Y4K0, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q9Y4K0, HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		ENSG00000134013, Low tissue specificity

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Component of some chromatin repressor complex.

    Interacts with SNAI1 (PubMed:16096638).

    Interacts with TAF10 (PubMed:25959397).

    Interacts with HSPA5 (PubMed:28332555).

    Interacts with EFEMP2 (PubMed:27339457).

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		110201, 39 interactors

    Protein interaction database and analysis system

    More...    IntActi    		Q9Y4K0, 32 interactors

    Molecular INTeraction database

    More...    MINTi    		Q9Y4K0

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000373783

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		Q9Y4K0

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		Q9Y4K0, protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1774
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		Q9Y4K0

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini58 – 159SRCR 1PROSITE-ProRule annotationAdd BLAST102
    Domaini188 – 302SRCR 2PROSITE-ProRule annotationAdd BLAST115
    Domaini326 – 425SRCR 3PROSITE-ProRule annotationAdd BLAST100
    Domaini435 – 544SRCR 4PROSITE-ProRule annotationAdd BLAST110

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni548 – 751Lysyl-oxidase likeAdd BLAST204

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The fourth SRCR domain plays an important role in optimizing the catalytic activity of the lysyl-oxidase like (LOX) catalytic domain.

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG502QSX8, Eukaryota

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000155874

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_002555_3_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q9Y4K0

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		YCTGKEA

    Database of Orthologous Groups

    More...    OrthoDBi    		815466at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q9Y4K0

    TreeFam database of animal gene trees

    More...    TreeFami    		TF326061

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.10.250.10, 4 hits

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001695, Lysyl_oxidase
    IPR019828, Lysyl_oxidase_CS
    IPR001190, SRCR
    IPR017448, SRCR-like_dom
    IPR036772, SRCR-like_dom_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01186, Lysyl_oxidase, 1 hit
    PF00530, SRCR, 4 hits

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00074, LYSYLOXIDASE
    PR00258, SPERACTRCPTR

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00202, SR, 4 hits

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF56487, SSF56487, 4 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00926, LYSYL_OXIDASE, 1 hit
    PS00420, SRCR_1, 2 hits
    PS50287, SRCR_2, 4 hits

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

    Q9Y4K0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP 
            60         70         80         90        100
    ANVAKIQLRL AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL 
           110        120        130        140        150
    GYVEAKSWTA SSSYGKGEGP IWLDNLHCTG NEATLAACTS NGWGVTDCKH 
           160        170        180        190        200
    TEDVGVVCSD KRIPGFKFDN SLINQIENLN IQVEDIRIRA ILSTYRKRTP 
           210        220        230        240        250
    VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER TYNTKVYKMF 
           260        270        280        290        300
    ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS 
           310        320        330        340        350
    CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV 
           360        370        380        390        400
    CDDKWDLVSA SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK 
           410        420        430        440        450
    SIIDCKFNAE SQGCNHEEDA GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV 
           460        470        480        490        500
    LVERNGSLVW GMVCGQNWGI VEAMVVCRQL GLGFASNAFQ ETWYWHGDVN 
           510        520        530        540        550
    SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG VACSETAPDL 
           560        570        580        590        600
    VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS 
           610        620        630        640        650
    SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE 
           660        670        680        690        700
    GHKASFCLED TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI 
           710        720        730        740        750
    TDVPPGDYLF QVVINPNFEV AESDYSNNIM KCRSRYDGHR IWMYNCHIGG 
           760        770 
    SFSEETEKKF EHFSGLLNNQ LSPQ
    Length:774
    Mass (Da):86,725
    Last modified:November 1, 1999 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9DF5D25D4824BCCD
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    E5RJL2E5RJL2_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		151Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RI22E5RI22_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		139Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RFE2E5RFE2_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		95Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YAR1H0YAR1_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		207Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RFY0E5RFY0_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		258Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RHH3E5RHH3_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		218Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YAP6H0YAP6_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		67Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    R4GMS2R4GMS2_HUMAN
    Lysyl oxidase homolog 2
    LOXL2
    		101Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAD34343 differs from that shown. Reason: Erroneous termination. Extended C-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti184E → K in BAG35197 (PubMed:14702039).Curated1
    Sequence conflicti239E → G in BAD96197 (Ref. 3) Curated1
    Sequence conflicti295L → Q in AAD34343 (PubMed:10212285).Curated1
    Sequence conflicti536Q → R in BAG35197 (PubMed:14702039).Curated1
    Sequence conflicti652H → Q in AAD34343 (PubMed:10212285).Curated1
    Sequence conflicti746C → S in AAD34343 (PubMed:10212285).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_050010359S → W. Corresponds to variant dbSNP:rs4602894Ensembl.1
    Natural variantiVAR_024527570M → L2 PublicationsCorresponds to variant dbSNP:rs1063582Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		U89942 mRNA Translation: AAB49697.1
    AK312266 mRNA Translation: BAG35197.1
    AK222477 mRNA Translation: BAD96197.1
    AC090197 Genomic DNA No translation available.
    BC000594 mRNA Translation: AAH00594.1
    AF117949 mRNA Translation: AAD34343.1 Sequence problems.

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS34864.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_002309.1, NM_002318.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000389131; ENSP00000373783; ENSG00000134013

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		4017

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:4017

    UCSC genome browser

    More...    UCSCi    		uc003xdh.2, human

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U89942 mRNA Translation: AAB49697.1
    AK312266 mRNA Translation: BAG35197.1
    AK222477 mRNA Translation: BAD96197.1
    AC090197 Genomic DNA No translation available.
    BC000594 mRNA Translation: AAH00594.1
    AF117949 mRNA Translation: AAD34343.1 Sequence problems.
    CCDSiCCDS34864.1
    RefSeqiNP_002309.1, NM_002318.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5ZE3X-ray2.40A/B318-774[»]
    SMRiQ9Y4K0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi110201, 39 interactors
    IntActiQ9Y4K0, 32 interactors
    MINTiQ9Y4K0
    STRINGi9606.ENSP00000373783

    Chemistry databases

    BindingDBiQ9Y4K0
    ChEMBLiCHEMBL3714029
    GuidetoPHARMACOLOGYi2853

    PTM databases

    GlyConnecti1480, 1 N-Linked glycan (1 site)
    GlyGeniQ9Y4K0, 3 sites
    iPTMnetiQ9Y4K0
    PhosphoSitePlusiQ9Y4K0

    Genetic variation databases

    BioMutaiLOXL2
    DMDMi13878585

    Proteomic databases

    EPDiQ9Y4K0
    jPOSTiQ9Y4K0
    MassIVEiQ9Y4K0
    MaxQBiQ9Y4K0
    PaxDbiQ9Y4K0
    PeptideAtlasiQ9Y4K0
    PRIDEiQ9Y4K0
    ProteomicsDBi86223

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...    ABCDi    		Q9Y4K0, 1 sequenced antibody

    Antibodypedia a portal for validated antibodies

    More...    Antibodypediai    		22758, 457 antibodies

    The DNASU plasmid repository

    More...    DNASUi    		4017

    Genome annotation databases

    EnsembliENST00000389131; ENSP00000373783; ENSG00000134013
    GeneIDi4017
    KEGGihsa:4017
    UCSCiuc003xdh.2, human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		4017
    DisGeNETi4017

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		LOXL2
    HGNCiHGNC:6666, LOXL2
    HPAiENSG00000134013, Low tissue specificity
    MIMi606663, gene
    neXtProtiNX_Q9Y4K0
    OpenTargetsiENSG00000134013
    PharmGKBiPA30429
    VEuPathDBiHostDB:ENSG00000134013.15

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiENOG502QSX8, Eukaryota
    GeneTreeiENSGT00940000155874
    HOGENOMiCLU_002555_3_0_1
    InParanoidiQ9Y4K0
    OMAiYCTGKEA
    OrthoDBi815466at2759
    PhylomeDBiQ9Y4K0
    TreeFamiTF326061

    Enzyme and pathway databases

    BRENDAi1.4.3.13, 2681
    PathwayCommonsiQ9Y4K0
    ReactomeiR-HSA-1566948, Elastic fibre formation
    R-HSA-2243919, Crosslinking of collagen fibrils
    SIGNORiQ9Y4K0

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...    BioGRID-ORCSi    		4017, 6 hits in 994 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		LOXL2, human

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		LOXL2

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		4017
    PharosiQ9Y4K0, Tbio

    Protein Ontology

    More...    PROi    		PR:Q9Y4K0
    RNActiQ9Y4K0, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000134013, Expressed in stromal cell of endometrium and 194 other tissues
    ExpressionAtlasiQ9Y4K0, baseline and differential
    GenevisibleiQ9Y4K0, HS

    Family and domain databases

    Gene3Di3.10.250.10, 4 hits
    InterProiView protein in InterPro
    IPR001695, Lysyl_oxidase
    IPR019828, Lysyl_oxidase_CS
    IPR001190, SRCR
    IPR017448, SRCR-like_dom
    IPR036772, SRCR-like_dom_sf
    PfamiView protein in Pfam
    PF01186, Lysyl_oxidase, 1 hit
    PF00530, SRCR, 4 hits
    PRINTSiPR00074, LYSYLOXIDASE
    PR00258, SPERACTRCPTR
    SMARTiView protein in SMART
    SM00202, SR, 4 hits
    SUPFAMiSSF56487, SSF56487, 4 hits
    PROSITEiView protein in PROSITE
    PS00926, LYSYL_OXIDASE, 1 hit
    PS00420, SRCR_1, 2 hits
    PS50287, SRCR_2, 4 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOXL2_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y4K0
    Secondary accession number(s): B2R5Q0
    , Q53HV3, Q9BW70, Q9Y5Y8
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1999
    Last modified: April 7, 2021
    This is version 190 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with genetic variants
      List of human entries with genetic variants
    3. Human variants curated from literature reports
      Index of human variants curated from literature reports
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again